Albumin Detection Service

Albumin is a multi-domain protein with significant structural stability, which functions as antioxidant and binding proteins. In addition, albumin helps the body to maintain colloidal osmotic pressure and acid-base homeostasis. Albumin is more sensitive to glycosylation than other proteins, and high glycated albumin (GA) levels are associated with some diseases and their complications, so albumin can be considered as a biomarker for diseases like diabetes mellitus and cirrhosis. Creative BioMart Biomarker offers high quality detection service for albumin, ensuring high detection accuracy, sensitivity and efficiency.


Albumin is the most abundant circulating protein in the human body, and its concentration of serum samples is generally in the range of 3.5 to 5.4 g/dL. Albumin accounts for 50-60% of total plasma protein and its molecular weight is 65-70 kDa. It is a negatively charged globular protein which is multifunctional and composed of approximately 585 amino acids. Albumin contains more than one lysine residue, arginine residue and cysteine residue, of which 17 disulfide bonds are formed from 34 cysteine residues, and these disulfide bonds are of great significance for the overall tertiary structure of albumin. In addition to the cysteine residues involved in the formation of disulfide bonds, there is also a free cysteine (Cys-34) in albumin, which is mainly present in the reduced form. Cys-34 makes albumin have the abilities of the antioxidant and scavenger. Albumin also functions as a binding protein, it is the major zinc-binding protein in plasma, and owns seven fatty acid binding sites, besides, albumin has a weaker ability to bind iron. Albumin is a heart- shaped protein composed of three similarly sized domains, and it contains six sub-domains, which are IA, IB, IIA, IIB, IIIA and IIIB. Furthermore, these sub-domains are related to the binding function of albumin. The half-life of albumin in plasma is as long as about 21 days because of its high structural stability, during which chemical structure changes may occur due to modifications such as peroxidation and non-enzymatic glycosylation, and these changes are related to the pathology of diabetes mellitus and cirrhosis. In addition to the above functions, albumin also has the function of maintaining colloid osmotic pressure and acid-base homeostasis. Decreased circulating levels of albumin in the body, or changes in the protein structure that affects its biochemical and physical properties may adversely affect the function of albumin.

Albumin Detection ServiceFigure 1. Molecular structure of human serum albumin (Arroyo, et al. 2014)

Application of Albumin Detection

  • Serum albumin level as a biomarker to predict different diseases, such as diabetes mellitus, cirrhosis, etc.

Our Advantages

  • Guarantee high accuracy and sensitivity for albumin detection
  • Ensure high repeatability of albumin detection
  • Short turn-around time of detection service
  • Competitive price in the market of detection services
  • Provide multiple albumin detection methods, including ELISA and automated colorimetric endpoint assay.
  • Accept a wide range of sample types (serum, urine, etc.)

Workflow of Albumin Detection at Creative BioMart Biomarker

Creative BioMart Biomarker strictly controls each specific experimental step in the albumin detection procedure to ensure accurately quantify the level of albumin in each sample.

Albumin Detection Service

At Creative BioMart Biomarker, we offer albumin detection service which includes several technical methods, you can communicate with our experts according to your research needs, and we will determine the final detection technological scheme based on the communication results. Please feel free to contact us, Creative BioMart Biomarker is here to offer you professional and thoughtful service.


  1. Arroyo, V.; et al. Human serum albumin, systemic inflammation, and cirrhosis. Journal of Hepatology. 2014, 61(2): 396-407.
  2. Dozio, E.; et al. Glycated albumin: from biochemistry and laboratory medicine to clinical practice. Endocrine. 2017, 55(3): 682-690.


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